Ala214,38]aprotinin: preparation by partial desulphurization of aprotinin by means of Raney nickel and comparison with other aprotinin derivatives

Schnabel, E.; Schröder, W.; Reinhardt, G.

Biological Chemistry Hoppe-Seyler 367(11): 1167-1176

1986


ISSN/ISBN: 0177-3593
PMID: 2434118
Accession: 004693561

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Abstract
Treatment of aprotinin with Raney nickel in the presence or absence of denaturants yielded .**GRAPHIC**. Aprotinin and .**GRAPHIC**. aprotinin were separated by ion exchange chromatography at pH 8 using Cm-Sepharose, fast flow. .**GRAPHIC**. aprotinin is a proteinase inhibitor, but it possesses lower affinities than aprotinin, for the enzymes trypsin, .alpha.-chymotrypsin, pancreatic kallikrein and plasmin as reflected by higher Ki values .**GRAPHIC**. aprotinin is slowly degraded by trypsin. The optical activity of .**GRAPHIC**. aprotininin different solvents is quite similar to that of aprotinin, or that of its hydrolysis products, [seco-15/16]aprotinin or [di-seco-15/16,39/40]-aprotinin. This is taken as good evidence for analogous molecular conformations of all these substrates.